Purification and partial molecular characterization of peroxidases in the rat intestine (EC 1.11.1.7)
Valoti, M.; Tipton, K.F.; Sgaragli, G.P.
Bollettino della Societa Italiana di Biologia Sperimentale 62(3): 335-340
1986
ISSN/ISBN: 0037-8771 PMID: 3013254 Document Number: 276865
Rat intestinal peroxidase (POD) was purified by a procedure involving gel-filtration on Sephacryl S-300, affinity chromatography on Con-A Sepharose and hydrophobic interaction chromatography on Phenyl-Sepharose. This preparation showed a specific activity of 93 Units .cntdot. mg-1 proteins, which was 640 fold higher than that exhibited by the initial crude homogenate, and a Soret index of 0.73. The enzyme appeared to be homogeneous by the criterion of polyacrylamide gel electrophoresis in presence of sodium dodecylsulfate and was characterized by a Mr of 48,000 daltons.